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Signal peptide peptidase (SPP) is an aspartyl protease that mediates clearance of signal peptides by proteolysis within the endoplasmic reticulum (ER). Like presenilins, SPP contains a critical GXGD motif in its C-terminal catalytic center. SPPL3 is one of several presenilin homologues/SPP-like proteins (PSHs/SPPL) that have been identified.
4833416I09Rik; fb94d08; Imp2; IMP-2; Intramembrane protease 2; MDHV1887; Presenilin homologous protein 1; presenilin-like protein 4; PRO4332; PSH1; PSL4; putative intramembrane aspartyl protease; RGD1562826; signal peptide peptidase 3; signal peptide peptidase like 3; signal peptide peptidase-like 3; signal peptide peptidase-like 3, pseudogene 1; Signal peptide peptidase-like 3-like protein; signal peptide peptidase-like protein 3; Sppl3; sppl3 protein; Sppl3-ps1; SPP-like 3; SPP-like 3 protein; upregulated during skeletal muscle growth 3; Usmg3; wu:fb94d08; zgc:114093
100 µg
100 µL
100 µL
100 µL